| dc.creator | Wachiratianchai,Supawadee | |
| dc.creator | Bhumiratana,Amaret | |
| dc.creator | Udomsopagit,Suchat | |
| dc.date | 2004-12-01 | |
| dc.date.accessioned | 2020-02-17T15:35:40Z | |
| dc.date.available | 2020-02-17T15:35:40Z | |
| dc.identifier | https://scielo.conicyt.cl/scielo.php?script=sci_arttext&pid=S0717-34582004000300009 | |
| dc.identifier.uri | https://revistaschilenas.uchile.cl/handle/2250/132016 | |
| dc.description | An extracellular L-glutamate oxidase (GLOD) was purified from soil-isolated Streptomyces sp 18G. The enzyme had a molecular weight of approximately 120,000 and consisted of two identical subunits, each with a molecular weight of 61,000. The isoelectric point was pH 8.5 and the enzyme had an optimal pH between 7.0-7.4. GLOD showed the maximum activity at 37ºC. The GLOD activity was stable at pH ranging from 6.5 to 7.0 for 1 hr. Among 21 amino acids tested for substrate specificity, L-glutamate was almost exclusively oxidized. D-glutamate and L-aspartate were oxidized but only to extents of 0.79% and 0.53%, respectively. | |
| dc.format | text/html | |
| dc.language | en | |
| dc.publisher | Pontificia Universidad Católica de Valparaíso | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.source | Electronic Journal of Biotechnology v.7 n.3 2004 | |
| dc.title | Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18G | |
